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Database: UniProt
Entry: A0A098EQR7_9BACL
LinkDB: A0A098EQR7_9BACL
Original site: A0A098EQR7_9BACL 
ID   A0A098EQR7_9BACL        Unreviewed;       570 AA.
AC   A0A098EQR7;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Gluconate 2-dehydrogenase flavoprotein {ECO:0000313|EMBL:CEG24130.1};
GN   ORFNames=BN1080_03150 {ECO:0000313|EMBL:CEG24130.1};
OS   Planococcus massiliensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX   NCBI_TaxID=1499687 {ECO:0000313|EMBL:CEG24130.1, ECO:0000313|Proteomes:UP000043699};
RN   [1] {ECO:0000313|EMBL:CEG24130.1, ECO:0000313|Proteomes:UP000043699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ES2 {ECO:0000313|EMBL:CEG24130.1,
RC   ECO:0000313|Proteomes:UP000043699};
RA   Urmite Genomes Urmite Genomes;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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DR   EMBL; CCXS01000001; CEG24130.1; -; Genomic_DNA.
DR   RefSeq; WP_052653398.1; NZ_LR698965.1.
DR   AlphaFoldDB; A0A098EQR7; -.
DR   STRING; 1499687.BN1080_03150; -.
DR   OrthoDB; 9787779at2; -.
DR   Proteomes; UP000043699; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR46056; LONG-CHAIN-ALCOHOL OXIDASE; 1.
DR   PANTHER; PTHR46056:SF4; LONG-CHAIN-ALCOHOL OXIDASE; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000043699}.
FT   DOMAIN          214..323
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          428..555
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
FT   REGION          161..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   570 AA;  63151 MW;  CD091A4DA7ACCC01 CRC64;
     MVTTLDKVDV VTVGVGWTGG IVAAECAKEG LKVVGLERGR ERGTEDFAIV HDEYRYAVRY
     ELMQDLSKET ITFRNRRDQK ALPMRQMGSF LLGEGLGGSG THWNGQNWRF LPYDFQIKTM
     TDEKYGANKL PPEYTIQDWG ITYDELEPYF DRFEKTAGIS GEDKNPFAGK RSSDYPTPPM
     KKTPILKKFE SATTNLGYSP FMMPSANLSE AYENPDGQQI NACQYCGFCE RFGCEYGAKT
     SPEITVVPTA KDTGNYEIKF NSNVVEIMKE GDRVTGVRYF DTVTFEEFIQ PAEVVVLTSY
     MLNNAKLLMV SEIGEMYDPE TGRGTLGKNY GYQILPGASG FFDEKMNVFM GAGALGMTID
     DFNGDNFDHS DLDFIHGASL SITQTGNRPI LTNPIPPDTP SWGADFKKAS IENYLKSLSI
     GGQGASMPHR DNYLSLDSTY KDIYGVPLLQ MTYNFTDQDR AMHKYVSERA AEIMQEMGAK
     TVVGGSPISD YDIVPYQTTH NTGGTIMGAE PETSVVNNYL QHWDMENLFV VGAGNFAHNG
     GYNPTGTVGA LAYRCAEGII NYSKNGGSLV
//
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